Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organism Marinibacillus marinus.

ABSTRACT: Adenylate kinases (AKs; EC 2.7.4.3) are essential members of the NMP kinase family that maintain cellular homeostasis by the interconversion of AMP, ADP and ATP. AKs play a critical role in adenylate homeostasis across all domains of life and have been used extensively as prototypes for the study of protein adaptation and the relationship of protein dynamics and stability to function. To date, kinetic studies of psychrophilic AKs have not been performed. In order to broaden understanding of extremophilic adaptation, the kinetic parameters of adenylate kinase from the psychrophile Marinibacillus marinus were examined and the crystal structure of this cold-adapted enzyme was determined at 2.0 A resolution. As expected, the overall structure and topology of the psychrophilic M. marinus AK are

SUBMITTER: Davlieva M 

PROVIDER: S-EPMC2720325 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature